Related ArticlesDetergent/Nanodisc screening for high-resolution NMR studies of an integral membrane protein containing a cytoplasmic domain.
PLoS One. 2013;8(1):e54378
Authors: Tzitzilonis C, Eichmann C, Maslennikov I, Choe S, Riek R
Abstract
Because membrane proteins need to be extracted from their natural environment and reconstituted in artificial milieus for the 3D structure determination by X-ray crystallography or NMR, the search for membrane mimetic that conserve the native structure and functional activities remains challenging. We demonstrate here a detergent/nanodisc screening study by NMR of the bacterial ?-helical membrane protein YgaP containing a cytoplasmic rhodanese domain. The analysis of 2D [(15)N,(1)H]-TROSY spectra shows that only a careful usage of low amounts of mixed detergents did not perturb the cytoplasmic domain while solubilizing in parallel the transmembrane segments with good spectral quality. In contrast, the incorporation of YgaP into nanodiscs appeared to be straightforward and yielded a surprisingly high quality [(15)N,(1)H]-TROSY spectrum opening an avenue for the structural studies of a helical membrane protein in a bilayer system by solution state NMR.
Micro-coil NMR to monitor optimization of the reconstitution conditions for the integral membrane protein OmpW in detergent micelles
Micro-coil NMR to monitor optimization of the reconstitution conditions for the integral membrane protein OmpW in detergent micelles
Abstract Optimization of aqueous solutions of the integral membrane protein (IMP) OmpW for NMR structure determination has been monitored with micro-coil NMR, which enables the acquisition of NMR spectra using only micrograms of protein and detergent. The detergent 30-Fos (2-undecylphosphocholine) was found to yield the best 2D -TROSY correlation NMR spectra of -labeled OmpW. For the OmpW structure determination we then optimized the 30-Fos concentration,...
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High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
Bioorg Chem. 2011 Feb;39(1):59-66
Authors: Borioni A, Bastanzio G, Delfini M, Mustazza C, Sciubba F, Tatti M, Del Giudice MR
The interaction of new bivalent NOP receptor antagonists with dodecyl phosphatidylcholine micelles and DMPC/cholesterol liposomes was investigated in solution by high resolution NMR. The ligands are...
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05-06-2011 02:00 AM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
J Am Chem Soc. 2011 Mar 1;
Authors: Renault M, Bos MP, Tommassen J, Baldus M
Multidomain proteins constitute a large part of prokaryotic and eukaryotic proteomes and play fundamental roles in various physiological processes. However, their structural characterization is challenging because of their large size and...
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03-03-2011 12:34 PM
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Protein Expr Purif. 2011 Feb 11;
Authors: Wang X, Gill Jr RL, Zhu Q, Tian F
LR11 (SorLA) is a recently identified neuronal protein that interacts with amyloid precursor protein (APP), a central player...
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02-16-2011 07:40 PM
[NMR paper] Solid-state NMR spectroscopic studies of an integral membrane protein inserted into a
Solid-state NMR spectroscopic studies of an integral membrane protein inserted into aligned phospholipid bilayer nanotube arrays.
Related Articles Solid-state NMR spectroscopic studies of an integral membrane protein inserted into aligned phospholipid bilayer nanotube arrays.
J Am Chem Soc. 2004 Aug 11;126(31):9504-5
Authors: Lorigan GA, Dave PC, Tiburu EK, Damodaran K, Abu-Baker S, Karp ES, Gibbons WJ, Minto RE
This communication demonstrates for the first time that solid-state NMR spectroscopic studies can be used to investigate aligned...
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[NMR paper] On choosing a detergent for solution NMR studies of membrane proteins.
On choosing a detergent for solution NMR studies of membrane proteins.
Related Articles On choosing a detergent for solution NMR studies of membrane proteins.
J Biomol NMR. 1998 May;11(4):381-6
Authors: Vinogradova O, Sönnichsen F, Sanders CR
Translational diffusion coefficients and catalytic activities were measured for the integral membrane protein diacylglycerol kinase (DAGK) in a variety of types of detergent micelles. Despite the structural diversity of the detergents examined, the translational diffusion coefficients observed for DAGK...
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[NMR paper] Detergent delipidation and solubilization strategies for high-resolution NMR of the m
Detergent delipidation and solubilization strategies for high-resolution NMR of the membrane protein bacteriorhodopsin.
Related Articles Detergent delipidation and solubilization strategies for high-resolution NMR of the membrane protein bacteriorhodopsin.
J Biol Chem. 1991 Jun 5;266(16):10066-9
Authors: Seigneuret M, Neumann JM, Rigaud JL
High-resolution NMR studies of bacteriorhodopsin require the availability of the detergent-solubilized protein with both high concentration and small rotational correlation time. A procedure is described for...
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[NMR paper] High resolution NMR for screening ligand/protein binding.
High resolution NMR for screening ligand/protein binding.
Related Articles High resolution NMR for screening ligand/protein binding.
Curr Opin Drug Discov Devel. 1999 Jul;2(4):396-400
Authors: Shapiro MJ, Wareing JR
High resolution NMR spectroscopy has provided a versatile tool for assessing ligand/receptor interactions. NMR-based methods are currently being investigated which may prove valuable for compound screening. These techniques include the use of chemical shift perturbations, the monitoring of translational diffusion and the...
Detergent/Nanodisc screening for high-resolution NMR studies of an integral membrane protein containing a cytoplasmic domain.
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